Purification and characterization of a kallikrein from human submaxillary glands.
A tissue kallikrein was purified over 1500-fold from the postmicrosomal supernatant of human submaxillary glands. The purified enzyme gave a single band, corresponding to an apparent molecular weight of 42,000 on SDS-polyacrylamide gel electrophoresis. This enzyme cross-reacted with the anti-human urinary kallikrein antiserum. The purified enzyme was characterized in comparison with the purest human urinary kallikrein preparation. Both enzymes hydrolyzed the synthetic substrate, Ac-Phe-Arg-OMe, most effectively. Aprotinin, TLCK, and PMSF suppressed the enzyme activities, while SBTI, LBTI, and alpha 1-antitrypsin had no effect at all. The purified enzyme generated kinin from the natural substrate, kininogen. It was concluded therefore that the purified enzyme is a typical tissue kallikrein.
Fujimoto
Y
Y
Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Japan.
Suzuki
C
C
Watanabe
Y
Y
Matsuda
Y
Y
Akihama
S
S
D000595:Amino Acid Sequence; D006801:Humans; D007120:Immunochemistry; D007610:Kallikreins / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009842:Oligopeptides; D013363:Submandibular Gland / Q000201:enzymology*; D013379:Substrate Specificity
D009842:Oligopeptides; D007610:Kallikreins